参考文献 References
[1] Whitaker, R., et al., Increased expression of Drosophila Sir2 extends life span in a dose-dependent manner. Aging (Albany NY), 2013. 5(9): p. 682-91.
[2] Li, Y., et al., A programmable fate decision landscape underlies single-cell aging in yeast. Science, 2020. 369(6501): p. 325-329.
[3] Nakagawa, T. and L. Guarente, Sirtuins at a glance. Journal of Cell Science, 2011. 124(6): p. 833-838.
[4] Michishita, E., et al., Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Molecular Biology of the Cell, 2005. 16(10): p. 4623-4635.
[5] Tsukamoto, Y., J. Kato, and H. Ikeda, Silencing factors participate in DNA repair and recombination in Saccharomyces cerevisiae. Nature, 1997. 388(6645): p. 900-903.
[6] Bonkowski, M.S. and D.A. Sinclair, Slowing ageing by design: the rise of NAD(+) and sirtuin-activating compounds. Nature Reviews Molecular Cell Biology, 2016. 17(11): p. 679-690.
[7] Choudhary, C., et al., Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions. Science, 2009. 325(5942): p. 834-840.
[8] Haigis, M.C. and D.A. Sinclair, Mammalian Sirtuins: Biological Insights and Disease Relevance. Annual Review of Pathology-Mechanisms of Disease, 2010. 5: p. 253-295.
[9] Panes, J.D., et al., Changes in PGC-1 alpha/SIRT1 Signaling Impact on Mitochondrial Homeostasis in Amyloid-Beta Peptide Toxicity Model. Frontiers in Pharmacology, 2020. 11.
[10] Chamberlain, K.A., et al., Oligodendrocytes enhance axonal energy metabolism by deacetylation of mitochondrial proteins through transcellular delivery of SIRT2. Neuron, 2021. 109(21): p. 3456-+.
[11] Lombard, D.B., et al., Mammalian sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation. Molecular and Cellular Biology, 2007. 27(24): p. 8807-8814.
[12] Chen, X.F., et al., SIRT5 inhibits peroxisomal ACOX1 to prevent oxidative damage and is downregulated in liver cancer. Embo Reports, 2018. 19(5).
[13] Roichman, A., et al., Restoration of energy homeostasis by SIRT6 extends healthy lifespan. Nature Communications, 2021. 12(1).
[14] Yan, W.W., et al., Arginine methylation of SIRT7 couples glucose sensing with mitochondria biogenesis. Embo Reports, 2018. 19(12).
[15] Shu, L., et al., ATAD3B is a mitophagy receptor mediating clearance of oxidative stress-induced damaged mitochondrial DNA. Embo Journal, 2021. 40(8).
[16] Ye, X., et al., Sirtuins in glucose and lipid metabolism. Oncotarget, 2017. 8(1): p. 1845-1859.
[17] Lee, I.H., et al., A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy. Proceedings of the National Academy of Sciences of the United States of America, 2008. 105(9): p. 3374-3379.
[18] Mu, N., et al., Inhibition of SIRT1/2 upregulates HSPA5 acetylation and induces pro-survival autophagy via ATF4-DDIT4-mTORC1 axis in human lung cancer cells. Apoptosis, 2019. 24(9-10): p. 798-811.
[19] Poole, L.P. and K.F. Macleod, Mitophagy in tumorigenesis and metastasis. Cellular and Molecular Life Sciences, 2021. 78(8): p. 3817-3851.
[20] Sun, Y., et al., Inhibition of nuclear deacetylase Sirtuin-1 induces mitochondrial acetylation and calcium overload leading to cell death. Redox Biology, 2022. 53.
[21] Tseng, A.H.H., S.S. Shieh, and D.L. Wang, SIRT3 deacetylates FOXO3 to protect mitochondria against oxidative damage. Free Radical Biology and Medicine, 2013. 63: p. 222-234.
[22] Longevity, O.M.C., Antiaging Properties of a Grape-Derived Antioxidant Are Regulated by Mitochondrial Balance of Fusion and Fission Leading to Mitophagy Triggered by a Signaling Network of Sirt1-Sirt3-Foxo3-PINK1-PARKIN (Retraction of Vol 2014, art no 345105, 2014). Oxidative Medicine and Cellular Longevity, 2022. 2022.
[23] Yu, L.M., et al., Polydatin attenuates chronic alcohol consumption-induced cardiomyopathy through a SIRT6-dependent mechanism. Food & Function, 2022. 13(13): p. 7302-7319.
[24] Ryu, D., et al., A SIRT7-Dependent Acetylation Switch of GABP beta 1 Controls Mitochondrial Function. Cell Metabolism, 2014. 20(5): p. 856-869.
[25] Hubbi, M.E., et al., Sirtuin-7 Inhibits the Activity of Hypoxia-inducible Factors. Journal of Biological Chemistry, 2013. 288(29): p. 20768-20775.
[26] Nguyen, T.T., et al., Loss of Miro1-directed mitochondrial movement results in a novel murine model for neuron disease. Proceedings of the National Academy of Sciences of the United States of America, 2014. 111(35): p. E3631-E3640.
[27] De Strooper, B. and E. Karran, The Cellular Phase of Alzheimer's Disease. Cell, 2016. 164(4): p. 603-615.
[28] Valla, J., et al., Reduced Posterior Cingulate Mitochondrial Activity in Expired Young Adult Carriers of the APOE epsilon 4 Allele, the Major Late-Onset Alzheimer's Susceptibility Gene. Journal of Alzheimers Disease, 2010. 22(1): p. 307-313.
[29] Mary, A., et al., Mitophagy in Alzheimer's disease: Molecular defects and therapeutic approaches. Molecular Psychiatry, 2022.
[30] Kobro-Flatmoen, A., et al., Re-emphasizing early Alzheimer's disease pathology starting in select entorhinal neurons, with a special focus on mitophagy. Ageing Research Reviews, 2021. 67.
[31] Chen, W.Y., et al., Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses. Cell, 2005. 123(3): p. 437-448.
[32] Kwon, H.S. and M. Oft, The ups and downs of SIRT1. Trends in Biochemical Sciences, 2008. 33(11): p. 517-525.
[33] Maiese, K., Targeting the core of neurodegeneration: FoxO, mTOR, and SIRT1. Neural Regeneration Research, 2021. 16(3): p. 448-455.
[34] Bai, N., et al., Inhibition of SIRT2 promotes APP acetylation and ameliorates cognitive impairment in APP/PS1 transgenic mice. Cell Reports, 2022. 40(2).
[35] Du, J.T., et al., Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase. Science, 2011. 334(6057): p. 806-809.
[36] Peng, C., et al., The First Identification of Lysine Malonylation Substrates and Its Regulatory Enzyme. Molecular & Cellular Proteomics, 2011. 10(12).
[37] Haigis, M.C., et al., SIRT4 inhibits glutamate dehydrogehase and opposes the effects of calorie restriction in pancreatic beta cells. Cell, 2006. 126(5): p. 941-954.
[38] Hirschey, M.D., et al., SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation. Nature, 2010. 464(7285): p. 121-U137.
[39] Giralt, A., et al., Peroxisome Proliferator-activated Receptor-gamma Coactivator-1 alpha Controls Transcription of the Sirt3 Gene, an Essential Component of the Thermogenic Brown Adipocyte Phenotype. Journal of Biological Chemistry, 2011. 286(19): p. 16958-16966.
[40] Jung, E.S., et al., p53-dependent SIRT6 expression protects A beta 42-induced DNA damage. Scientific Reports, 2016. 6.